SSB_BPT4
ID SSB_BPT4 Reviewed; 301 AA.
AC P03695; Q38555;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Single-stranded DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04152};
DE Short=SSB protein {ECO:0000255|HAMAP-Rule:MF_04152};
DE AltName: Full=Gp32 {ECO:0000255|HAMAP-Rule:MF_04152};
DE AltName: Full=Helix-destabilizing protein {ECO:0000255|HAMAP-Rule:MF_04152};
GN Name=32 {ECO:0000255|HAMAP-Rule:MF_04152}; Synonyms=ssb;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (AMBER MUTANT 32AMA453).
RX PubMed=6289325; DOI=10.1073/pnas.79.16.4937;
RA Krisch H.M., Allet B.;
RT "Nucleotide sequences involved in bacteriophage T4 gene 32 translational
RT self-regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:4937-4941(1982).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=6257686; DOI=10.1016/s0021-9258(19)69872-8;
RA Williams K.R., Lopresti M.B., Setoguchi M.;
RT "Primary structure of the bacteriophage T4 DNA helix-destabilizing
RT protein.";
RL J. Biol. Chem. 256:1754-1762(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [4]
RP PRELIMINARY PROTEIN SEQUENCE OF 1-74 AND 94-282.
RX PubMed=6997174; DOI=10.1515/bchm2.1980.361.2.1139;
RA Pan Y.-C.E., Nakashima Y., Sharief F.S., Li S.S.-L.;
RT "Amino acid sequence studies on T4 gene 32 DNA-binding proteins.";
RL Hoppe-Seyler's Z. Physiol. Chem. 361:1139-1153(1980).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-301 (MUTANT DELTA PR201).
RX PubMed=8429554; DOI=10.1006/jmbi.1993.1042;
RA Hurley J.M., Chervitz S.A., Jarvis T.C., Singer B.S., Gold L.;
RT "Assembly of the bacteriophage T4 replication machine requires the acidic
RT carboxy terminus of gene 32 protein.";
RL J. Mol. Biol. 229:398-418(1993).
RN [6]
RP ZINC-BINDING.
RX PubMed=1731933; DOI=10.1021/bi00118a018;
RA Giedroc D.P., Qiu H., Khan R., King G.C., Chen K.;
RT "Zn(II) coordination domain mutants of T4 gene 32 protein.";
RL Biochemistry 31:765-774(1992).
RN [7]
RP DOMAIN.
RX PubMed=1736285; DOI=10.1073/pnas.89.3.1050;
RA Casas-Finet J.R., Fischer K.R., Karpel R.L.;
RT "Structural basis for the nucleic acid binding cooperativity of
RT bacteriophage T4 gene 32 protein: the (Lys/Arg)3(Ser/Thr)2 (LAST) motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1050-1054(1992).
RN [8]
RP INTERACTION WITH THE DNA HELICASE ASSEMBLY PROTEIN.
RX PubMed=7806533; DOI=10.1016/s0021-9258(20)30096-x;
RA Barry J., Alberts B.;
RT "Purification and characterization of bacteriophage T4 gene 59 protein. A
RT DNA helicase assembly protein involved in DNA replication.";
RL J. Biol. Chem. 269:33049-33062(1994).
RN [9]
RP FUNCTION.
RX PubMed=9079662; DOI=10.1074/jbc.272.13.8380;
RA Kong D., Nossal N.G., Richardson C.C.;
RT "Role of the bacteriophage T7 and T4 single-stranded DNA-binding proteins
RT in the formation of joint molecules and DNA helicase-catalyzed polar branch
RT migration.";
RL J. Biol. Chem. 272:8380-8387(1997).
RN [10]
RP REVIEW.
RX PubMed=11459967; DOI=10.1073/pnas.131007498;
RA Bleuit J.S., Xu H., Ma Y., Wang T., Liu J., Morrical S.W.;
RT "Mediator proteins orchestrate enzyme-ssDNA assembly during T4
RT recombination-dependent DNA replication and repair.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8298-8305(2001).
RN [11]
RP FUNCTION, AND INTERACTION WITH THE DNA HELICASE ASSEMBLY PROTEIN.
RX PubMed=15507125; DOI=10.1186/1743-422x-1-4;
RA Borjac-Natour J.M., Petrov V.M., Karam J.D.;
RT "Divergence of the mRNA targets for the Ssb proteins of bacteriophages T4
RT and RB69.";
RL Virol. J. 1:4-4(2004).
RN [12]
RP FUNCTION.
RX PubMed=14871889; DOI=10.1074/jbc.m311738200;
RA Ma Y., Wang T., Villemain J.L., Giedroc D.P., Morrical S.W.;
RT "Dual functions of single-stranded DNA-binding protein in helicase loading
RT at the bacteriophage T4 DNA replication fork.";
RL J. Biol. Chem. 279:19035-19045(2004).
RN [13]
RP IDENTIFICATION IN THE REPLICASE COMPLEX.
RX PubMed=16800624; DOI=10.1021/bi0603322;
RA Smiley R.D., Zhuang Z., Benkovic S.J., Hammes G.G.;
RT "Single-molecule investigation of the T4 bacteriophage DNA polymerase
RT holoenzyme: multiple pathways of holoenzyme formation.";
RL Biochemistry 45:7990-7997(2006).
RN [14]
RP INTERACTION WITH SF2 UVSW HELICASE.
RX PubMed=23732982; DOI=10.1016/j.jmb.2013.05.012;
RA Perumal S.K., Nelson S.W., Benkovic S.J.;
RT "Interaction of T4 UvsW helicase and single-stranded DNA binding protein
RT gp32 through its carboxy-terminal acidic tail.";
RL J. Mol. Biol. 425:2823-2839(2013).
RN [15]
RP INTERACTION WITH THE DNA HELICASE ASSEMBLY PROTEIN.
RX PubMed=24338568; DOI=10.1074/jbc.m113.505842;
RA Branagan A.M., Klein J.A., Jordan C.S., Morrical S.W.;
RT "Control of helicase loading in the coupled DNA replication and
RT recombination systems of bacteriophage T4.";
RL J. Biol. Chem. 289:3040-3054(2014).
RN [16]
RP DOMAIN, AND INTERACTION WITH THE DNA HELICASE.
RX PubMed=25481875; DOI=10.1016/j.dnarep.2014.10.002;
RA Jordan C.S., Morrical S.W.;
RT "Regulation of the bacteriophage T4 Dda helicase by Gp32 single-stranded
RT DNA-binding protein.";
RL DNA Repair 25:41-53(2015).
RN [17]
RP SUBUNIT.
RX PubMed=26275775; DOI=10.1093/nar/gkv817;
RA Jose D., Weitzel S.E., Baase W.A., von Hippel P.H.;
RT "Mapping the interactions of the single-stranded DNA binding protein of
RT bacteriophage T4 (gp32) with DNA lattices at single nucleotide resolution:
RT gp32 monomer binding.";
RL Nucleic Acids Res. 43:9276-9290(2015).
RN [18]
RP REVIEW.
RX PubMed=26102578; DOI=10.3390/v7062766;
RA Noble E., Spiering M.M., Benkovic S.J.;
RT "Coordinated DNA replication by the bacteriophage T4 replisome.";
RL Viruses 7:3186-3200(2015).
RN [19]
RP DOMAIN.
RX PubMed=29634784; DOI=10.1371/journal.pone.0194357;
RA Pant K., Anderson B., Perdana H., Malinowski M.A., Win A.T., Pabst C.,
RA Williams M.C., Karpel R.L.;
RT "The role of the C-domain of bacteriophage T4 gene 32 protein in ssDNA
RT binding and dsDNA helix-destabilization: Kinetic, single-molecule, and
RT cross-linking studies.";
RL PLoS ONE 13:e0194357-e0194357(2018).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-239.
RX PubMed=7630406; DOI=10.1038/376362a0;
RA Shamoo Y., Friedman A.M., Parsons M.R., Konigsberg W.H., Steitz T.A.;
RT "Crystal structure of a replication fork single-stranded DNA binding
RT protein (T4 gp32) complexed to DNA.";
RL Nature 376:362-366(1995).
RN [21]
RP ERRATUM OF PUBMED:7630406.
RA Shamoo Y., Friedman A.M., Parsons M.R., Konigsberg W.H., Steitz T.A.;
RL Nature 376:616-616(1995).
CC -!- FUNCTION: Single-stranded DNA-binding protein that participates in
CC viral DNA replication, recombination, and repair (Probable). Coats the
CC lagging-strand ssDNA as the replication fork advances (PubMed:9079662).
CC Stimulates the activities of viral DNA polymerase and DnaB-like SF4
CC replicative helicase, probably via its interaction with the helicase
CC assembly factor (PubMed:14871889). Together with DnaB-like SF4
CC replicative helicase and the helicase assembly factor, promotes pairing
CC of two homologous DNA molecules containing complementary single-
CC stranded regions and mediates homologous DNA strand exchange
CC (PubMed:11459967). Promotes also the formation of joint molecules
CC (PubMed:9079662). mRNA specific autogenous translational repressor
CC (PubMed:15507125). {ECO:0000255|HAMAP-Rule:MF_04152,
CC ECO:0000269|PubMed:11459967, ECO:0000269|PubMed:14871889,
CC ECO:0000269|PubMed:15507125, ECO:0000269|PubMed:9079662,
CC ECO:0000305|PubMed:9079662}.
CC -!- SUBUNIT: Homodimer in the absence of DNA, monomer when binding DNA
CC (PubMed:26275775). Interacts with the DNA helicase assembly protein; a
CC ternary complex between the helicase assembly protein, the single-
CC stranded DNA-binding protein and ssDNA is an obligatory intermediate in
CC the helicase loading mechanism (PubMed:24338568, PubMed:15507125). Part
CC of the replicase complex that includes the DNA polymerase, the
CC polymerase clamp, the clamp loader complex, the single-stranded DNA
CC binding protein, the primase, the DnaB-like SF4 replicative helicase
CC and the helicase assembly factor (PubMed:16800624, PubMed:26102578).
CC Interacts (via C-terminus) with the viral SF1 dDA helicase
CC (PubMed:25481875). Interacts with the viral SF2 UvsW repair helicase
CC (PubMed:23732982). {ECO:0000255|HAMAP-Rule:MF_04152,
CC ECO:0000269|PubMed:15507125, ECO:0000269|PubMed:16800624,
CC ECO:0000269|PubMed:23732982, ECO:0000269|PubMed:24338568,
CC ECO:0000269|PubMed:25481875, ECO:0000269|PubMed:26275775,
CC ECO:0000303|PubMed:26102578}.
CC -!- DOMAIN: The acidic C-terminus is involved in modulating the ssDNA
CC binding properties (PubMed:29634784). The N-terminus LAST motif is
CC involved in the cooperative binding of the protein to ssDNA
CC (PubMed:1736285). {ECO:0000255|HAMAP-Rule:MF_04152,
CC ECO:0000269|PubMed:1736285, ECO:0000269|PubMed:29634784}.
CC -!- SIMILARITY: Belongs to the Tequatrovirus single-stranded DNA-binding
CC protein family. {ECO:0000255|HAMAP-Rule:MF_04152}.
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DR EMBL; J02513; AAA32511.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42454.1; -; Genomic_DNA.
DR EMBL; S54962; AAB25300.1; -; Genomic_DNA.
DR PIR; A93924; DDBP34.
DR RefSeq; NP_049854.1; NC_000866.4.
DR PDB; 1GPC; X-ray; 2.20 A; A=22-239.
DR PDBsum; 1GPC; -.
DR SMR; P03695; -.
DR GeneID; 1258602; -.
DR KEGG; vg:1258602; -.
DR EvolutionaryTrace; P03695; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.90.198.10; -; 1.
DR HAMAP; MF_04152; SSB_T4; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012339; Phage_T4_Gp32_ssDNA-bd.
DR InterPro; IPR044947; Phage_T4_Gp32_ssDNA-bd_sf.
DR InterPro; IPR046395; SSB_T4.
DR Pfam; PF08804; gp32; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA repair;
KW DNA replication; DNA-binding; Metal-binding; Reference proteome; Repressor;
KW Viral DNA replication; Zinc.
FT CHAIN 1..301
FT /note="Single-stranded DNA-binding protein"
FT /id="PRO_0000165047"
FT REGION 3..7
FT /note="LAST"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04152,
FT ECO:0000269|PubMed:1736285"
FT REGION 272..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04152,
FT ECO:0000269|PubMed:1731933"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04152,
FT ECO:0000269|PubMed:1731933"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04152,
FT ECO:0000269|PubMed:1731933"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04152,
FT ECO:0000269|PubMed:1731933"
FT VARIANT 116..301
FT /note="Missing (in mutant 32AMA453)"
FT /evidence="ECO:0000269|PubMed:6289325"
FT VARIANT 292..296
FT /note="Missing (in mutant delta PR201)"
FT /evidence="ECO:0000269|PubMed:8429554"
FT CONFLICT 86
FT /note="S -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 276..277
FT /note="DD -> NN (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1GPC"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:1GPC"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1GPC"
FT STRAND 57..68
FT /evidence="ECO:0007829|PDB:1GPC"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1GPC"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:1GPC"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:1GPC"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:1GPC"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:1GPC"
FT STRAND 112..123
FT /evidence="ECO:0007829|PDB:1GPC"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1GPC"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1GPC"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:1GPC"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1GPC"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1GPC"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1GPC"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:1GPC"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1GPC"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:1GPC"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:1GPC"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:1GPC"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:1GPC"
SQ SEQUENCE 301 AA; 33506 MW; 4C9771CF5D978487 CRC64;
MFKRKSTAEL AAQMAKLNGN KGFSSEDKGE WKLKLDNAGN GQAVIRFLPS KNDEQAPFAI
LVNHGFKKNG KWYIETCSST HGDYDSCPVC QYISKNDLYN TDNKEYSLVK RKTSYWANIL
VVKDPAAPEN EGKVFKYRFG KKIWDKINAM IAVDVEMGET PVDVTCPWEG ANFVLKVKQV
SGFSNYDESK FLNQSAIPNI DDESFQKELF EQMVDLSEMT SKDKFKSFEE LNTKFGQVMG
TAVMGGAAAT AAKKADKVAD DLDAFNVDDF NTKTEDDFMS SSSGSSSSAD DTDLDDLLND
L
